ArticleNucleic acids research2001
14-3-3tau associates with and activates the MEF2D transcription factor during muscle cell differentiation.
Article in Nucleic acids research, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 17 citations in OpenAlex.
- The Dual Functions of Andrographolide in the Epstein-Barr Virus-Positive Head-and-Neck Cancer Cells: The Inhibition of Lytic Reactivation of the Epstein-Barr Virus and the Induction of Cell Death.International journal of molecular sciences · 2023Article
- Involvement of myocyte enhancer factor 2c in the pathogenesis of autism spectrum disorder.Heliyon · 2021Review
- WRINKLED1 as a novel 14-3-3 client: function of 14-3-3 proteins in plant lipid metabolism.Plant signaling & behavior · 2018Article
- B Cell Receptor Activation Predominantly Regulates AKT-mTORC1/2 Substrates Functionally Related to RNA Processing.PloS one · 2016Article
- Histone deacetylases in kidney development: implications for disease and therapy.Pediatric nephrology (Berlin, Germany) · 2013Review
- Histone deacetylases (HDACs): characterization of the classical HDAC family.The Biochemical journal · 2003Review
- Statistical significance of clusters of motifs represented by position specific scoring matrices in nucleotide sequences.Nucleic acids research · 2002Article
- MEF2-mediated recruitment of class II HDAC at the EBV immediate early gene BZLF1 links latency and chromatin remodeling.EMBO reports · 2002Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Myocyte enhancer binding factor 2 (MEF2) proteins belong to the MADS box family of transcription factors and four MEF2 proteins, MEF2A, MEF2B, MEF2C and MEF2D, have been found. MEF2 proteins have been shown to play critical roles in differentiation of muscles and neuronal tissues. How transactivational activity of MEF2 proteins is regulated is not fully understood. MEF2 proteins are activated by several kinases, including Erk5 and calcium/calmodulin-dependent kinase, and interact with repressors, including histone deacetylases 4 and 5 (HDAC4 and HDAC5) and Cabin1. During the effort to understand regulation of MEF2 activity, we identified 14-3-3tau as a MEF2D-interacting molecule by yeast two-hybrid screening. We found that 14-3-3tau forms a complex with MEF2D in vivo and specifically enhances MEF2 transactivational activity. The results from transient transfection and co-precipitation experiments suggest that 14-3-3tau activates MEF2D by competitively inhibiting HDAC4 from binding to MEF2D and thereby affects muscle cell differentiation.
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